ID   MIPA_ECOLI              Reviewed;         248 AA.
AC   P0A908; O07962; P77486;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   07-JAN-2015, entry version 78.
DE   RecName: Full=MltA-interacting protein;
DE   Flags: Precursor;
GN   Name=mipA; Synonyms=yeaF; OrderedLocusNames=b1782, JW1771;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 23-35, AND INTERACTION WITH MLTA AND MRCB/PONB.
RC   STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX   PubMed=10037771; DOI=10.1074/jbc.274.10.6726;
RA   Vollmer W., von Rechenberg M., Hoeltje J.-V.;
RT   "Demonstration of molecular interactions between the murein polymerase
RT   PBP1B, the lytic transglycosylase MltA, and the scaffolding protein
RT   MipA of Escherichia coli.";
RL   J. Biol. Chem. 274:6726-6734(1999).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10806384; DOI=10.1046/j.1432-1327.2000.01296.x;
RA   Molloy M.P., Herbert B.R., Slade M.B., Rabilloud T., Nouwens A.S.,
RA   Williams K.L., Gooley A.A.;
RT   "Proteomic analysis of the Escherichia coli outer membrane.";
RL   Eur. J. Biochem. 267:2871-2881(2000).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.M506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
CC   -!- FUNCTION: May serve as a scaffold protein required for the
CC       formation of a complex with MrcB/PonB and MltA, this complex could
CC       play a role in enlargement and septation of the murein sacculus.
CC   -!- SUBUNIT: Forms a trimeric complex with MrcB and MltA in vitro.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000269|PubMed:16079137}.
CC   -!- SIMILARITY: Belongs to the MipA/OmpV family. {ECO:0000305}.
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DR   EMBL; U00096; AAC74852.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15579.1; -; Genomic_DNA.
DR   PIR; F64938; F64938.
DR   RefSeq; NP_416296.1; NC_000913.3.
DR   RefSeq; YP_490043.1; NC_007779.1.
DR   ProteinModelPortal; P0A908; -.
DR   IntAct; P0A908; 4.
DR   STRING; 511145.b1782; -.
DR   TCDB; 9.B.99.1.2; the mipa-interacting protein (mipa) family.
DR   PRIDE; P0A908; -.
DR   EnsemblBacteria; AAC74852; AAC74852; b1782.
DR   EnsemblBacteria; BAA15579; BAA15579; BAA15579.
DR   GeneID; 12931317; -.
DR   GeneID; 946301; -.
DR   KEGG; ecj:Y75_p1757; -.
DR   KEGG; eco:b1782; -.
DR   PATRIC; 32118875; VBIEscCol129921_1855.
DR   EchoBASE; EB3265; -.
DR   EcoGene; EG13492; mipA.
DR   eggNOG; COG3713; -.
DR   HOGENOM; HOG000121141; -.
DR   InParanoid; P0A908; -.
DR   KO; K07274; -.
DR   OMA; LSIMAYY; -.
DR   OrthoDB; EOG6ZKXQ0; -.
DR   PhylomeDB; P0A908; -.
DR   BioCyc; EcoCyc:G6968-MONOMER; -.
DR   BioCyc; ECOL316407:JW1771-MONOMER; -.
DR   PRO; PR:P0A908; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   Genevestigator; P0A908; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030674; F:protein binding, bridging; IPI:EcoCyc.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IPI:EcoCyc.
DR   InterPro; IPR010583; MipA.
DR   InterPro; IPR017690; OM_insertion_C_omp85_target.
DR   Pfam; PF06629; MipA; 1.
DR   TIGRFAMs; TIGR03304; OMP85_target; 3.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Complete proteome; Direct protein sequencing;
KW   Membrane; Reference proteome; Signal.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:10037771}.
FT   CHAIN        23    248       MltA-interacting protein.
FT                                /FTId=PRO_0000019092.
FT   CONFLICT     34     34       V -> N (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   248 AA;  27831 MW;  6571B0D7A47A0525 CRC64;
     MTKLKLLALG VLIATSAGVA HAEGKFSLGA GVGVVEHPYK DYDTDVYPVP VINYEGDNFW
     FRGLGGGYYL WNDATDKLSI TAYWSPLYFK AKDSGDHQMR HLDDRKSTMM AGLSYAHFTQ
     YGYLRTTLAG DTLDNSNGIV WDMAWLYRYT NGGLTVTPGI GVQWNSENQN EYYYGVSRKE
     SARSGLRGYN PNDSWSPYLE LSASYNFLGD WSVYGTARYT RLSDEVTDSP MVDKSWTGLI
     STGITYKF
//